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- EMDB-1871: Three-dimensional model of Salmonella's needle complex at subnano... -
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Open data
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Basic information
Entry | Database: EMDB / ID: EMD-1871 | |||||||||
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Title | Three-dimensional model of Salmonella's needle complex at subnanometer resolution | |||||||||
![]() | This in an image of a the surface rendered, extracted volume of the lower neck (15 fold) of the needle complex of the type III secretion system from Salmonella tyhpimurium. | |||||||||
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![]() | Type III secretion system / Salmonella / outer membrane ring / secretin family / C15 fold | |||||||||
Function / homology | ![]() type III protein secretion system complex / type II protein secretion system complex / protein secretion by the type III secretion system / protein secretion / cell outer membrane / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 8.3 Å | |||||||||
![]() | Schraidt O / Marlovits TC | |||||||||
![]() | ![]() Title: Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Authors: Oliver Schraidt / Thomas C Marlovits / ![]() Abstract: Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core ...Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core structure, the needle complex (NC), is a ~3.5 megadalton-sized, oligomeric, membrane-embedded complex. Analyzing cryo-electron microscopy images of top views of NCs or NC substructures from Salmonella typhimurium revealed a 24-fold symmetry for the inner rings and a 15-fold symmetry for the outer rings, giving an overall C3 symmetry. Local refinement and averaging showed the organization of the central core and allowed us to reconstruct a subnanometer composite structure of the NC, which together with confident docking of atomic structures reveal insights into its overall organization and structural requirements during assembly. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 17.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 8.2 KB 8.2 KB | Display Display | ![]() |
Images | ![]() | 757.6 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 206.5 KB | Display | ![]() |
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Full document | ![]() | 205.7 KB | Display | |
Data in XML | ![]() | 6.5 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 2y9kMC ![]() 1874C ![]() 1875C ![]() 2y9jC C: citing same article ( M: atomic model generated by this map |
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Similar structure data |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
File | ![]() | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
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Annotation | This in an image of a the surface rendered, extracted volume of the lower neck (15 fold) of the needle complex of the type III secretion system from Salmonella tyhpimurium. | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 1.33 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : Needle complex from Salmonella typhimurium
Entire | Name: Needle complex from Salmonella typhimurium |
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Components |
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-Supramolecule #1000: Needle complex from Salmonella typhimurium
Supramolecule | Name: Needle complex from Salmonella typhimurium / type: sample / ID: 1000 / Number unique components: 1 |
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-Macromolecule #1: Protein invG
Macromolecule | Name: Protein invG / type: protein_or_peptide / ID: 1 / Name.synonym: invG / Recombinant expression: No |
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Source (natural) | Organism: ![]() |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.5 / Details: 10mM Tris-HCl 0.5M NaCl 0.1% LDAO |
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Vitrification | Cryogen name: ETHANE / Instrument: OTHER |
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Electron microscopy
Microscope | FEI POLARA 300 |
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Image recording | Digitization - Sampling interval: 15 µm / Bits/pixel: 8 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 93000 |
Sample stage | Specimen holder: Eucentric / Specimen holder model: GATAN LIQUID NITROGEN |
Experimental equipment | ![]() Model: Tecnai Polara / Image courtesy: FEI Company |
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Image processing
CTF correction | Details: Micrograph |
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Final reconstruction | Applied symmetry - Point group: C15 (15 fold cyclic) / Algorithm: OTHER / Resolution.type: BY AUTHOR / Resolution: 8.3 Å / Resolution method: FSC 0.5 CUT-OFF / Software - Name: IMAGIC |
-Atomic model buiding 1
Initial model | PDB ID: Chain - Chain ID: A |
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Details | Protocol: Rigid body. Based on the homolog EscC (PDB entry above) a model was built for InvG (Swissprot - template based modeling), which was subsequently used for the fitting experiment (rigid body, Software CHIMERA) |
Refinement | Space: REAL / Protocol: RIGID BODY FIT |
Output model | ![]() PDB-2y9k: |